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基本情報
登録情報 | データベース: PDB / ID: 6c3p | ||||||
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タイトル | Cryo-EM structure of human KATP bound to ATP and ADP in propeller form | ||||||
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![]() | TRANSPORT PROTEIN / ATP-dependent potassium channel Kir6.2 SUR1 ATP ADP | ||||||
機能・相同性 | ![]() Defective ABCC9 causes CMD10, ATFB12 and Cantu syndrome / negative regulation of neuroblast migration / positive regulation of uterine smooth muscle relaxation / ATP sensitive Potassium channels / Defective ABCC8 can cause hypo- and hyper-glycemias / positive regulation of tight junction disassembly / potassium ion-transporting ATPase complex / negative regulation of blood-brain barrier permeability / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission ...Defective ABCC9 causes CMD10, ATFB12 and Cantu syndrome / negative regulation of neuroblast migration / positive regulation of uterine smooth muscle relaxation / ATP sensitive Potassium channels / Defective ABCC8 can cause hypo- and hyper-glycemias / positive regulation of tight junction disassembly / potassium ion-transporting ATPase complex / negative regulation of blood-brain barrier permeability / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / inward rectifying potassium channel / negative regulation of low-density lipoprotein particle clearance / sulfonylurea receptor activity / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / positive regulation of potassium ion transport / inward rectifier potassium channel activity / ATPase-coupled monoatomic cation transmembrane transporter activity / regulation of monoatomic ion transmembrane transport / response to pH / inorganic cation transmembrane transport / nervous system process / neuromuscular process / ankyrin binding / negative regulation of glial cell proliferation / response to ATP / : / response to zinc ion / voltage-gated potassium channel activity / intracellular glucose homeostasis / potassium channel activity / potassium ion import across plasma membrane / positive regulation of insulin secretion involved in cellular response to glucose stimulus / potassium ion binding / regulation of insulin secretion / ATPase-coupled transmembrane transporter activity / negative regulation of insulin secretion / ABC-type transporter activity / Ion homeostasis / potassium ion transmembrane transport / T-tubule / negative regulation of angiogenesis / regulation of membrane potential / Regulation of insulin secretion / female pregnancy / visual learning / potassium ion transport / response to insulin / ABC-family proteins mediated transport / sarcolemma / memory / transmembrane transport / ADP binding / synaptic vesicle membrane / glucose metabolic process / positive regulation of tumor necrosis factor production / transmembrane transporter binding / response to lipopolysaccharide / response to xenobiotic stimulus / ATP hydrolysis activity / ATP binding / membrane / plasma membrane 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 5.6 Å | ||||||
![]() | Lee, K.P.K. / Chen, J. / MacKinnon, R. | ||||||
![]() | ![]() タイトル: Molecular structure of human KATP in complex with ATP and ADP. 著者: Kenneth Pak Kin Lee / Jue Chen / Roderick MacKinnon / ![]() 要旨: In many excitable cells, KATP channels respond to intracellular adenosine nucleotides: ATP inhibits while ADP activates. We present two structures of the human pancreatic KATP channel, containing the ...In many excitable cells, KATP channels respond to intracellular adenosine nucleotides: ATP inhibits while ADP activates. We present two structures of the human pancreatic KATP channel, containing the ABC transporter SUR1 and the inward-rectifier K channel Kir6.2, in the presence of Mg and nucleotides. These structures, referred to as quatrefoil and propeller forms, were determined by single-particle cryo-EM at 3.9 Å and 5.6 Å, respectively. In both forms, ATP occupies the inhibitory site in Kir6.2. The nucleotide-binding domains of SUR1 are dimerized with Mg-ATP in the degenerate site and Mg-ADP in the consensus site. A lasso extension forms an interface between SUR1 and Kir6.2 adjacent to the ATP site in the propeller form and is disrupted in the quatrefoil form. These structures support the role of SUR1 as an ADP sensor and highlight the lasso extension as a key regulatory element in ADP's ability to override ATP inhibition. | ||||||
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構造の表示
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構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 1.1 MB | 表示 | ![]() |
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PDB形式 | ![]() | 932.3 KB | 表示 | ![]() |
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-検証レポート
文書・要旨 | ![]() | 1.5 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.7 MB | 表示 | |
XML形式データ | ![]() | 186.9 KB | 表示 | |
CIF形式データ | ![]() | 276.6 KB | 表示 | |
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-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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要素
#1: タンパク質 | 分子量: 45144.367 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #2: タンパク質 | 分子量: 177180.219 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #3: 化合物 | ChemComp-ATP / #4: 化合物 | ChemComp-ADP / #5: 化合物 | ChemComp-MG / |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
構成要素 | 名称: Quatrefoil form of human KATP in complex with ATP and ADP タイプ: COMPLEX / Entity ID: #1-#2 / 由来: RECOMBINANT |
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分子量 | 値: 0.88 MDa / 実験値: NO |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() |
緩衝液 | pH: 8.5 |
試料 | 濃度: 0.45 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | グリッドの材料: GOLD / グリッドのサイズ: 400 divisions/in. / グリッドのタイプ: Quantifoil R1.2/1.3 |
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 283 K |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD |
撮影 | 電子線照射量: 1.18 e/Å2 / 検出モード: SUPER-RESOLUTION フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
EMソフトウェア |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3次元再構成 | 解像度: 5.6 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 47282 / 対称性のタイプ: POINT |